Sialylation and sialyltransferase in insects.

Glycoconj J

School of Biological Sciences, National Institute of Science Education and Research (NISER), Bhubaneswar, Odisha, 752050, India.

Published: October 2018

Sialic acids are negatively charged nine carbon monosaccharides located terminally on glycoproteins and glycolipids that control cellular physiological processes. Sialylation is a post translational modification (ptm) regulated by enzymes and has been studied in prokaryotes including bacteria, dueterostomes including vertebrates, Cephalochordates, Ascidians, Echinoderms and protostomes including Molluscs and Arthropods and Plant. Although diverse structures of sialylated molecules have been reported in different organisms, unravelling sialylation in insect biology is a completely new domain. Within protostomes, the study of sialylation in members of Phylum Arthropoda and Class Insecta finds importance. Reports on sialylation in some insects exist. Genetically engineered components of sialylation pathway in Spodoptera frugiperda (Sf9) cell lines have enabled our understanding of sialylation and expression of mammalian proteins in insects. In this study we have summarised the finding on (i) sialylated molecules (ii) processes and enzymes involved (iii) function of sialylation (iv) genetic engineering approaches and generation of mammalian protein expression systems (v) a comparison of sialylation machinery in insects with that of mammals (vi) genes and transcriptional regulation in insects. At present no information on structural studies of insect sialyltransferase (STs) exist. We report minor differences in ST structure in insects on complete protein sequences recorded in Genbank through in silico approaches. An indepth study of all the components of the sialylation pathway in different insect species across different families and their evolutionary significance finds importance as the future scope of this review.

Download full-text PDF

Source
http://dx.doi.org/10.1007/s10719-018-9835-6DOI Listing

Publication Analysis

Top Keywords

sialylation
10
sialylated molecules
8
components sialylation
8
sialylation pathway
8
insects
6
sialylation sialyltransferase
4
sialyltransferase insects
4
insects sialic
4
sialic acids
4
acids negatively
4

Similar Publications

Structure-Function Relationships of the CMP-Sialic Acid Transporter through Analysis of a Pathogenic Variant in an Alternatively Spliced Functional Isoform.

ACS Omega

December 2024

Laboratorio de Glicobiología y Diagnóstico Molecular, Centro de Investigación en Dinámica Celular, Universidad Autónoma del Estado de Morelos, Av. Universidad 1001, Col. Chamilpa, Cuernavaca 62209, Morelos, México.

The human CMP-sialic acid transporter (hCST) is a mammalian highly conserved type III antiporter that translocates CMP-sialic acid into the Golgi lumen, supporting sialylation. Although different works have focused on elucidating structure-function relationships in the hCST, this is the first study to address them in an alternatively spliced isoform. We have previously reported the expression of a functional human del177 isoform that has skipping of exon 6, resulting in a loss of 59 amino acids, without change in the open reading frame and conserving its C-terminal region.

View Article and Find Full Text PDF

The CHO VRC01 cell line produces an anti-HIV IgG1 monoclonal antibody containing N-linked glycans on both the Fab (variable) and Fc (constant) regions. Site-specific glycan analysis was used to measure the complex effects of cell culture process conditions on Fab and Fc glycosylation. Experimental data revealed major differences in glycan fractions across the two sites.

View Article and Find Full Text PDF

Parasitic infections during pregnancy in Gabon affect glycosylation patterns of maternal and child antibodies.

Sci Rep

December 2024

Leiden University Center for Infectious Diseases (LUCID), Leiden University Medical Center (LUMC), Albinusdreef 2, 2333ZA, Leiden, Zuid-Holland, The Netherlands.

Antibody glycosylation patterns can affect antibody functionality and thereby contribute to protection against invading pathogens. During pregnancy, maternal antibodies can be transferred through the placenta and contribute to modulating both the mother's and her child's immune responses. Although several studies of IgG glycosylation during pregnancy have been carried out, very few cohorts studied were from sub-Saharan Africa, where exposure to microorganisms and parasites is high.

View Article and Find Full Text PDF

Surface-enhanced Raman spectroscopy as effective tool for detection of sialic acid as cancer biomarker.

Spectrochim Acta A Mol Biomol Spectrosc

December 2024

Department of Chemistry, Indian Institute of Technology Roorkee, Roorkee 247667, Uttarakhand, India. Electronic address:

Sialic acid, a negatively charged nine-carbon monosaccharide, is mainly located at the terminal end of glycan chains on glycoproteins and glycolipids of cell surface and most secreted proteins. Elevated levels of sialylated glycans have been known as a hallmark in numerous cancers. As a result, sialic acid acts as a useful and accessible cancer biomarker for early cancer detection and monitoring the disease development during cancer treatment which is crucial in elevating the survival rate.

View Article and Find Full Text PDF

Comprehensive site- and structure-specific profiling of N-glycosylation of edible bird's nest (EBN) proteome using label-free quantitative glycoproteomics.

Food Chem

December 2024

Chinese Academy of Inspection and Quarantine, Beijing 100176, People's Republic of China. Electronic address:

Glycoproteins, which are involved in numerous biological functions, are among the most critical functional ingredients in an edible bird's nest (EBN). To gain a comprehensive understanding of the glycoprotein species within EBN, a label-free, site-specific glycoproteomic approach was used to analyze their N-glycoproteins, N-glycopeptides, and N-glycans systematically. A total of 127 N-glycoproteins were identified in EBN, of which 72 were found in house-EBN and 63 in cave-EBN, yielding 4195 and 5649 glycopeptides, respectively.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!